› 6nm1

X-ray diffraction
2.33Å resolution

The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein A158L mutant to 2.33 Angstrom resolution exhibits a conformation change compared to the wild type form

Released:
DOI: 10.2210/pdb6nm1/pdb
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PDB entry 6nm1 coloured by chain, front view.
PDB entry 6nm1 coloured by chain, side view.
PDB entry 6nm1 coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Identification of structural transitions in bacterial fatty acid binding proteins that permit ligand entry and exit at membranes.
Gullett JM, Cuypers MG, Grace CR, Pant S, Subramanian C, Tajkhorshid E, Rock CO, White SW
OpenAccess logo J Biol Chem 298 101676 (2022)
PMID: 35122790

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DegV domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 32.14 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A0N2 (Residues: 1-288; Coverage: 100%)
Sequence domains: Uncharacterised protein, DegV family COG1307

Ligands and Environments

1 bound ligand:
Ligand MYR 2 x MYR
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P1
Unit cell:
a: 33.355Å b: 53.517Å c: 86.152Å
α: 76.88° β: 89.36° γ: 72.27°
R-values:
R R work R free
0.24 0.237 0.288
Expression system: Escherichia coli

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Citations

1 review citation

Interfacial Enzymes Enable Gram-Positive Microbes to Eat Fatty Acids.
Radka CD. (2023)
5 other articles

1 mention without citation

Identification of structural transitions in bacterial fatty acid binding proteins that permit ligand entry and exit at membranes.
Gullett et al. (2022)

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